1ga5
From Proteopedia
(New page: 200px<br /> <applet load="1ga5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ga5, resolution 2.40Å" /> '''CRYSTAL STRUCTURE O...) |
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| - | [[Image:1ga5.gif|left|200px]]<br /> | + | [[Image:1ga5.gif|left|200px]]<br /><applet load="1ga5" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ga5" size=" | + | |
caption="1ga5, resolution 2.40Å" /> | caption="1ga5, resolution 2.40Å" /> | ||
'''CRYSTAL STRUCTURE OF THE ORPHAN NUCLEAR RECEPTOR REV-ERB(ALPHA) DNA-BINDING DOMAIN BOUND TO ITS COGNATE RESPONSE ELEMENT'''<br /> | '''CRYSTAL STRUCTURE OF THE ORPHAN NUCLEAR RECEPTOR REV-ERB(ALPHA) DNA-BINDING DOMAIN BOUND TO ITS COGNATE RESPONSE ELEMENT'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Most nuclear receptors recognize the same consensus hexameric sequence, AGGTCA. An important question has been how the various members of this | + | Most nuclear receptors recognize the same consensus hexameric sequence, AGGTCA. An important question has been how the various members of this transcription factor family distinguish identity features in these closely related DNA sites. We determined structures from several crystal forms of the RevErb-DNA complex and analyzed the patterns of protein-DNA interactions and DNA distortions. We found a significant and consistent DNA distortion at a TA step directly preceding the first consensus 5'-AGGTCA-3' recognition sequence. Importantly, while this base-pair sequence is associated with RevErb's high-affinity sites, there are no sequence-specific contacts formed with the protein. Our study shows that RevErb relies instead on the intrinsic geometry and flexibility of this TA site to make the required fit between the proteins' independent major groove and minor groove binding interactions, which occur on both sides of the TA step. Our findings extend the description of response element discrimination to include a role for sequence-dependent DNA deformations and suggest how other monomeric members of this superfamily, such as NGFI-B, SF-1, and ROR, could also recognize unique geometric features in their DNA targets. |
==About this Structure== | ==About this Structure== | ||
| - | 1GA5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1GA5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GA5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Rastinejad, F.]] | [[Category: Rastinejad, F.]] | ||
| - | [[Category: Sierk, M | + | [[Category: Sierk, M L.]] |
[[Category: Zhao, Q.]] | [[Category: Zhao, Q.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: reverb]] | [[Category: reverb]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:47:53 2008'' |
Revision as of 10:47, 21 February 2008
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CRYSTAL STRUCTURE OF THE ORPHAN NUCLEAR RECEPTOR REV-ERB(ALPHA) DNA-BINDING DOMAIN BOUND TO ITS COGNATE RESPONSE ELEMENT
Overview
Most nuclear receptors recognize the same consensus hexameric sequence, AGGTCA. An important question has been how the various members of this transcription factor family distinguish identity features in these closely related DNA sites. We determined structures from several crystal forms of the RevErb-DNA complex and analyzed the patterns of protein-DNA interactions and DNA distortions. We found a significant and consistent DNA distortion at a TA step directly preceding the first consensus 5'-AGGTCA-3' recognition sequence. Importantly, while this base-pair sequence is associated with RevErb's high-affinity sites, there are no sequence-specific contacts formed with the protein. Our study shows that RevErb relies instead on the intrinsic geometry and flexibility of this TA site to make the required fit between the proteins' independent major groove and minor groove binding interactions, which occur on both sides of the TA step. Our findings extend the description of response element discrimination to include a role for sequence-dependent DNA deformations and suggest how other monomeric members of this superfamily, such as NGFI-B, SF-1, and ROR, could also recognize unique geometric features in their DNA targets.
About this Structure
1GA5 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
DNA deformability as a recognition feature in the reverb response element., Sierk ML, Zhao Q, Rastinejad F, Biochemistry. 2001 Oct 30;40(43):12833-43. PMID:11669620
Page seeded by OCA on Thu Feb 21 12:47:53 2008
Categories: Homo sapiens | Single protein | Rastinejad, F. | Sierk, M L. | Zhao, Q. | ZN | Dna-binding | Nuclear receptor | Orphan receptor | Rev-erb | Reverb
